A mechanistic study supports a two-step mechanism for peptide bond formation on the ribosome

被引：11

作者：

Byun, Byung Jin ^{[1
]}

Kang, Young Kee ^{[1
]}

机构：

[1] Chungbuk Natl Univ, Dept Chem, Cheongju 361763, Chungbuk, South Korea

来源：

PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2013年 / 15卷 / 36期

基金：

新加坡国家研究基金会;

关键词：

SUBSTRATE-ASSISTED CATALYSIS; TRANSITION-STATE; DENSITY FUNCTIONALS; STRUCTURAL INSIGHTS; TRANSFERASE CENTER; SITE; STABILIZATION; 2'-HYDROXYL; KINETICS; REVEALS;

D O I：

10.1039/c3cp51082d

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We report the feasible pathways of the quaternary model system for the ribosome-catalyzed PT reaction obtained by density functional calculations. Our results indicate that the step from the reactant complex to the first six-membered TS involving a proton shuttle via the 2'-OH of the P-site A76 in the stepwise pathway is the most favored rate-limiting step in solution. It is found that the C-O3' bond-breaking of A76 is not significant but the C-N bond formation with a tetrahedral intermediate occurs in the rate-limiting step and that the fast breakdown of the C-O3' bond is followed in the second transition state. These are consistent with recent kinetic experiments.

引用

页码：14931 / 14935

页数：5

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